Prieto J C, Carmena M J
Cell Biochem Funct. 1987 Jan;5(1):63-8. doi: 10.1002/cbf.290050108.
The binding of [125I]-human growth hormone (hGH) was studied in epithelial cells isolated from rat ventral prostate. Binding and degradation were dependent on time and temperature. The effect of a lysosomotropic agent suggested internalization and lysosomal degradation of the hormone. Dissociation and stoichiometric studies indicated the existence of a single class of GH receptors with a Kd of 0.7 nM and a binding capacity of 46 fmol hGH bound mg-1 cell protein. The receptor appeared to possess a somatotrophic nature since lactogenic hormones such as human placental lactogen and rat prolactin exhibited a very low degree of competition (whereas a variety of unrelated hormones and neuropeptides showed no effect). GH-stimulated leucine uptake by the cells in a time- and dose-dependent manner, half maximal effect being observed at 0.32 nM GH thus suggesting a direct relationship with the binding step.
对从大鼠腹侧前列腺分离的上皮细胞中[125I] - 人生长激素（hGH）的结合进行了研究。结合和降解取决于时间和温度。一种溶酶体促渗剂的作用表明该激素发生内化和溶酶体降解。解离和化学计量学研究表明存在一类单一的GH受体，其解离常数（Kd）为0.7 nM，结合能力为46 fmol hGH结合mg-1细胞蛋白。该受体似乎具有促生长特性，因为人胎盘催乳素和大鼠催乳素等催乳激素表现出非常低的竞争程度（而各种不相关的激素和神经肽则无作用）。GH以时间和剂量依赖性方式刺激细胞对亮氨酸的摄取，在0.32 nM GH时观察到半数最大效应，因此表明与结合步骤存在直接关系。
